Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3FRF

S. aureus DHFR complexed with NADPH and iclaprim

Functional Information from GO Data
ChainGOidnamespacecontents
X0004146molecular_functiondihydrofolate reductase activity
X0006730biological_processone-carbon metabolic process
X0016491molecular_functionoxidoreductase activity
X0046654biological_processtetrahydrofolate biosynthetic process
X0050661molecular_functionNADP binding
Functional Information from PDB Data
site_idAC1
Number of Residues27
DetailsBINDING SITE FOR RESIDUE NDP X 301
ChainResidue
XVAL6
XLYS45
XTHR46
XLEU62
XTHR63
XSER64
XHIS77
XILE79
XPHE92
XGLY93
XGLY94
XALA7
XGLN95
XTHR96
XLEU97
XGLU100
XTHR121
XHOH176
XHOH177
XXCF300
XILE14
XGLY15
XASN18
XGLN19
XLEU20
XGLY43
XARG44

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE XCF X 300
ChainResidue
XLEU5
XVAL6
XALA7
XLEU20
XASP27
XLEU28
XVAL31
XSER49
XLEU54
XPHE92
XHOH167
XHOH253
XNDP301

Functional Information from PROSITE/UniProt
site_idPS00075
Number of Residues23
DetailsDHFR_1 Dihydrofolate reductase (DHFR) domain signature. VIGfenqLPWhlpn.DlkhVkklS
ChainResidueDetails
XVAL13-SER35

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000305|PubMed:19280600
ChainResidueDetails
XLEU5
XASP27
XSER49
XARG57
XPHE92

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19280600
ChainResidueDetails
XVAL6
XILE14
XGLY43
XLEU62
XGLU100
XTHR121

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon